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@ARTICLE{Sun:644614,
      author       = {Sun, Xun and Saha, Debasis and Wang, Xue and Mörman,
                      Cecilia and Sternke-Hoffmann, Rebecca and Gerez, Juan Atilio
                      and Herranz-Trillo, Fátima and Riek, Roland and Zheng,
                      Wenwei and Luo, Jinghui},
      title        = {{S}permine modulation of {A}lzheimer’s {T}au and
                      {P}arkinson’s α-synuclein: implications for biomolecular
                      condensation and neurodegeneration},
      journal      = {Nature Communications},
      volume       = {16},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Springer Nature},
      reportid     = {PUBDB-2026-00447},
      pages        = {10239},
      year         = {2025},
      abstract     = {Spermine, a pivotal player in biomolecular condensation and
                      diverse cellular processes, has emerged as a focus of
                      investigation in aging, neurodegeneration, and other
                      diseases. Despite its significance, the mechanistic details
                      of spermine remain incompletely understood. Here, we
                      describe the distinct modulation by spermine on
                      Alzheimer’s Tau and Parkinson’s α-synuclein,
                      elucidating their condensation behaviors in vitro and in
                      vivo. Using biophysical techniques including time-resolved
                      SAXS and NMR, we trace electrostatically driven transitions
                      from atomic-scale conformational changes to mesoscopic
                      structures. Notably, spermine extends lifespan, ameliorates
                      movement deficits, and restores mitochondrial function in C.
                      elegans models expressing Tau and α-synuclein. Acting as a
                      molecular glue, spermine orchestrates in vivo condensation
                      of α-synuclein, influences condensate mobility, and
                      promotes degradation via autophagy, specifically through
                      autophagosome expansion. This study unveils the interplay
                      between spermine, protein condensation, and functional
                      outcomes, advancing our understanding of neurodegenerative
                      diseases and paving the way for therapeutic development.},
      cin          = {EMBL-User},
      ddc          = {500},
      cid          = {I:(DE-H253)EMBL-User-20120814},
      pnm          = {6G3 - PETRA III (DESY) (POF4-6G3)},
      pid          = {G:(DE-HGF)POF4-6G3},
      experiment   = {EXP:(DE-H253)P-P12-20150101},
      typ          = {PUB:(DE-HGF)16},
      doi          = {10.1038/s41467-025-65426-3},
      url          = {https://bib-pubdb1.desy.de/record/644614},
}